5OL2
The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0009055 | molecular_function | electron transfer activity |
A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
A | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0009055 | molecular_function | electron transfer activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0009055 | molecular_function | electron transfer activity |
D | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
D | 0046872 | molecular_function | metal ion binding |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0009055 | molecular_function | electron transfer activity |
F | 0000166 | molecular_function | nucleotide binding |
F | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
F | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | binding site for residue FAD A 401 |
Chain | Residue |
A | GLY216 |
A | GLN259 |
A | THR260 |
A | GLY261 |
A | GLY273 |
A | ILE274 |
A | SER275 |
A | GLY276 |
A | ALA277 |
A | GLN279 |
A | HIS280 |
A | ARG217 |
A | ASN294 |
A | LYS295 |
A | GLY311 |
A | ASP312 |
A | VAL313 |
C | THR343 |
C | TYR346 |
F | PRO127 |
F | GLU198 |
A | GLY218 |
A | SER242 |
A | ARG243 |
A | ALA244 |
A | GLN256 |
A | VAL257 |
A | GLY258 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CA A 402 |
Chain | Residue |
A | GLU75 |
A | ASP188 |
site_id | AC3 |
Number of Residues | 23 |
Details | binding site for residue FAD B 300 |
Chain | Residue |
A | LEU116 |
A | THR117 |
A | ARG136 |
A | ILE147 |
B | CYS11 |
B | ILE12 |
B | LYS13 |
B | ASP43 |
B | MET66 |
B | ALA97 |
B | ASP98 |
B | THR99 |
B | THR102 |
B | ALA120 |
B | GLY121 |
B | ALA124 |
B | GLY127 |
B | ASP128 |
B | THR129 |
B | ALA130 |
B | GLN131 |
B | VAL132 |
B | THR227 |
site_id | AC4 |
Number of Residues | 23 |
Details | binding site for residue FAD C 401 |
Chain | Residue |
C | PHE122 |
C | LEU124 |
C | THR125 |
C | GLY130 |
C | THR131 |
C | PHE155 |
C | ILE156 |
C | THR157 |
C | GLN278 |
C | ILE357 |
C | TYR361 |
C | GLU362 |
C | THR364 |
C | GLU366 |
C | COS402 |
F | ARG267 |
F | GLN269 |
F | PHE270 |
F | LEU274 |
F | GLN335 |
F | LEU336 |
F | GLY338 |
F | GLY339 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue COS C 402 |
Chain | Residue |
B | ASP24 |
B | THR27 |
C | THR131 |
C | SER134 |
C | PHE231 |
C | MET235 |
C | LEU238 |
C | ARG242 |
C | GLU362 |
C | GLY363 |
C | FAD401 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CA C 403 |
Chain | Residue |
C | GLU29 |
C | GLU33 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CA D 402 |
Chain | Residue |
D | GLU75 |
D | ASP188 |
site_id | AC8 |
Number of Residues | 25 |
Details | binding site for residue FAD E 301 |
Chain | Residue |
E | MET66 |
E | ALA97 |
E | ASP98 |
E | THR99 |
E | THR102 |
E | ALA120 |
E | GLY121 |
E | ARG122 |
E | GLN123 |
E | ALA124 |
E | GLY127 |
E | ASP128 |
E | THR129 |
E | ALA130 |
E | GLN131 |
E | VAL132 |
E | THR227 |
D | LEU116 |
D | THR117 |
D | ARG136 |
D | ILE147 |
E | CYS11 |
E | ILE12 |
E | LYS13 |
E | ASP43 |
site_id | AC9 |
Number of Residues | 23 |
Details | binding site for residue FAD F 401 |
Chain | Residue |
C | ARG267 |
C | PHE270 |
C | LEU274 |
C | PHE277 |
C | GLN335 |
C | LEU336 |
C | GLY338 |
C | GLY339 |
F | PHE122 |
F | LEU124 |
F | THR125 |
F | GLY130 |
F | THR131 |
F | PHE155 |
F | ILE156 |
F | THR157 |
F | GLN278 |
F | ILE357 |
F | TYR361 |
F | GLU362 |
F | THR364 |
F | GLU366 |
F | COS402 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue COS F 402 |
Chain | Residue |
F | THR125 |
F | THR131 |
F | MET235 |
F | LEU238 |
F | ARG242 |
F | LYS276 |
F | GLU362 |
F | GLY363 |
F | MET370 |
F | FAD401 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue CA F 403 |
Chain | Residue |
F | GLU29 |
F | GLU33 |
F | ARG35 |
site_id | AD3 |
Number of Residues | 30 |
Details | binding site for Di-peptide FAD D 401 and ASN D 294 |
Chain | Residue |
C | PRO127 |
C | GLU198 |
D | GLY216 |
D | ARG217 |
D | GLY218 |
D | SER242 |
D | ARG243 |
D | ALA244 |
D | GLN256 |
D | VAL257 |
D | GLY258 |
D | GLN259 |
D | THR260 |
D | GLY261 |
D | GLY273 |
D | ILE274 |
D | SER275 |
D | GLY276 |
D | ALA277 |
D | GLN279 |
D | HIS280 |
D | ILE293 |
D | LYS295 |
D | ASN296 |
D | ILE309 |
D | VAL310 |
D | GLY311 |
D | VAL313 |
F | THR343 |
F | TYR346 |
site_id | AD4 |
Number of Residues | 32 |
Details | binding site for Di-peptide FAD D 401 and HIS D 280 |
Chain | Residue |
C | PRO127 |
C | GLU198 |
D | GLY216 |
D | ARG217 |
D | GLY218 |
D | SER242 |
D | ARG243 |
D | ALA244 |
D | GLN256 |
D | VAL257 |
D | GLY258 |
D | GLN259 |
D | THR260 |
D | GLY261 |
D | TYR269 |
D | GLY273 |
D | ILE274 |
D | SER275 |
D | GLY276 |
D | ALA277 |
D | ILE278 |
D | GLN279 |
D | ILE281 |
D | ALA282 |
D | GLY283 |
D | ASN294 |
D | LYS295 |
D | ASN296 |
D | GLY311 |
D | VAL313 |
F | THR343 |
F | TYR346 |
Functional Information from PROSITE/UniProt
site_id | PS00072 |
Number of Residues | 13 |
Details | ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. GLTEpnAGTDasG |
Chain | Residue | Details |
C | GLY123-GLY135 |
site_id | PS00073 |
Number of Residues | 20 |
Details | ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QlHGGyGYtrDypveRmmrD |
Chain | Residue | Details |
C | GLN335-ASP354 |
site_id | PS00696 |
Number of Residues | 27 |
Details | ETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYIAcGISGaIQHiaGmedaefIvAIN |
Chain | Residue | Details |
A | LEU268-ASN294 |